Current Proteomics

Author(s): Ramar Perumal Samy, Ponnampalam Gopalakrishnakone, Seetharama D. Satyanarayanajois, Bradley G. Stiles and Vincent T. K. Chow

DOI: 10.2174/1570164611310010003

Snake Venom Proteins and Peptides as Novel Antibiotics Against Microbial Infections

Page: [10 - 28] Pages: 19

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Abstract

Animals produce a large variety of antimicrobial peptides that play an important role in natural innate immunity and controlling microbial infections. Snakes are classified into the phylum Chordata and class Reptilia, within the animal kingdom. Snake venoms are extensive mixtures that contain a large number of biologically active proteins/ peptides that represent a promising source of potential therapeutics for both humans and animals. These components are extensively studied for a wide range of pharmacological properties; however, it is quite exceptional that very little is relatively known about antimicrobial activity associated with venoms to date. In this review, we emphasize the available literature linked to antimicrobial activity of venom proteins such as L-amino acid oxidase (LAAO), phospholipase A2 (PLA2), peptides and snake cathelicidin. We propose a model for antimicrobial action in comparison with existing mechanisms. Structure and function of snake venom proteins/peptides in relation to antimicrobial activity and its involvement in molecular pharmacology thoroughly discussed. Nevertheless, snake venom enzymes and various classes of peptides have unique pharmacological properties, enhanced properties of antimicrobial effects against various bacterial infections, as well as varying levels of toxicity on eukaryotic and prokaryotic cells. In conclusions, these peptide-based molecules may ultimately be used as alternative drugs to replace chemical antibiotics that increasingly become less useful due to highly-evolved resistance mechanisms employed by various microbial pathogens.

Keywords: Antibiotics, antimicrobial peptides, L-amino acid oxidase, microbial infections, phospholipase A2, snake cathelicidin